3n5k: Difference between revisions
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==Structure Of The (Sr)Ca2+-ATPase E2-AlF4- Form== | ==Structure Of The (Sr)Ca2+-ATPase E2-AlF4- Form== | ||
<StructureSection load='3n5k' size='340' side='right' caption='[[3n5k]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='3n5k' size='340' side='right' caption='[[3n5k]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xp5|1xp5]], [[3b9r|3b9r]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xp5|1xp5]], [[3b9r|3b9r]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3n5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n5k RCSB], [http://www.ebi.ac.uk/pdbsum/3n5k PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3n5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n5k OCA], [http://pdbe.org/3n5k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n5k RCSB], [http://www.ebi.ac.uk/pdbsum/3n5k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n5k ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3n5k" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 10:25, 4 August 2016
Structure Of The (Sr)Ca2+-ATPase E2-AlF4- FormStructure Of The (Sr)Ca2+-ATPase E2-AlF4- Form
Structural highlights
Function[AT2A1_RABIT] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity). Publication Abstract from PubMedThe sarco(endo)plasmic reticulum Ca2+- ATPase (SERCA) is a transmembrane ion transporter belonging to the PII-type ATPases. It performs the vital task of re-sequestering cytoplasmic Ca2+ to the sarco-endoplasmic reticulum store, thereby also terminating Ca2+-induced signaling such as in muscle contraction. This article focuses on the transport pathways of Ca2+ and H+ ions across the lipid bilayer through SERCA. The ion binding sites of SERCA are accessible from either the cytoplasm or the SR/ER lumen at a time, and the Ca2+ entry and exit channels are both formed mainly by rearrangements of four N-terminal transmembrane (TM) alpha-helices. Recent improvements in the resolution of the crystal structures of rabbit SERCA1a have revealed a hydrated pathway in the Cterminal TM region leading from the ion binding sites to the cytosol. A comparison of different SERCA conformations reveals that this C-terminal pathway is exclusive to Ca2+- free E2-states, suggesting that it may play a functional role in proton release from the ion binding sites. This is in agreement with molecular dynamics (MD) simulations, mutational studies, and in striking analogy to a similar pathway recently described for the related sodium pump. We therefore suggest a model for the ion exchange mechanism in PII-ATPases including not only one, but two cytoplasmic pathways working in concert. Ion pathways in the sarcoplasmic reticulum Ca2+-ATPase.,Bublitz M, Musgaard M, Poulsen H, Thogersen L, Olesen C, Schiott B, Morth JP, Moller JV, Nissen P J Biol Chem. 2013 Feb 11. PMID:23400778[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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